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The crystal structure of an FMN-dependent NADH-azoreductase, azoa in complex with red 40
Analyse The crystal structure of an FMN-dependent NADH-azoreductase, azoa in complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7N2W
- Type
- protein
- Length
- 804 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A6TCS9
- Ligands
- FMN, 05G
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D | — | protein | 201 | — | A6TCS9 |
| B | — | protein | 202 | — | A6TCS9 |
| C | — | protein | 200 | — | A6TCS9 |
Ligands and binding sites
- FMN · Flavin mononucleotide · ligand · 4 copies · chains A, B, C, D
- 05G · 6-hydroxy-5-[(E)-(2-methoxy-5-methyl-4-sulfophenyl) diazenyl]naphthalene-2-sulfonic acid · ligand · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7N2W · The crystal structure of an FMN-dependent NADH-azoreductase, AzoA in complex with Red 40 · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt A6TCS9
- Elsewhere: RCSB PDB 7N2W · PDBe 7N2W · UniProt A6TCS9
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